Four 9-kDa proteins excreted by somatic embryos of grapevine are isoforms of lipid-transfer proteins

• Published in: European Journal of Biochemistry Vol. 217; no. 3; pp. 885 - 889
• Main Authors: Coutos-Thevenot, P, Jouenne, T, Maes, O, Guerbette, F, Grosbois, M, Le Caer, J.P, Boulay, M, Deloire, A, Kader, J.C, Guern, J
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.11.1993; Blackwell; Wiley
• Subjects: Amino Acid Sequence; amino acid sequences; Analytical, structural and metabolic biochemistry; Antigens, Plant; Binding and carrier proteins; Biological and medical sciences; Carrier Proteins - chemistry; Carrier Proteins - isolation & purification; Cells, Cultured; Chromatography, Ion Exchange; comparisons; Electrophoresis, Polyacrylamide Gel; Fruit - chemistry; Fundamental and applied biological sciences. Psychology; genbank; Life Sciences; Molecular Sequence Data; plant proteins; Plant Proteins - chemistry; Plant Proteins - isolation & purification; protein secretion; Proteins; Seeds - chemistry; Sequence Homology, Amino Acid; somatic embryogenesis; Vitis; Vitis cinerea var. helleri; Vitis vinifera; Phospholipid transfer protein; Cell culture; Embryo; Molecular form; Purification; Vitis; Somatic cell; Biological activity; Vitidaceae; Dicotyledones; Angiospermae; Spermatophyta; Aminoacid sequence; Structural analysis
• ISSN: 0014-2956; 1432-1033; 1432-1327
• DOI: 10.1111/j.1432-1033.1993.tb18317.x

Four 9-kDa small extracellular proteins produced by embryogenic cultures in the absence of auxin have been purified from the extracellular medium of grapevine somatic embryo cultures through cation-exchange chromatography and hydrophobic-interaction chromatography. The partial amino-acid sequences reflect high similarities between the four proteins as well as with the sequences established for carrot, spinach, millet and maize nonspecific lipid-transfer proteins. All these sequences show conservation of three cysteines at positions 4, 14 and 30-32, as well as glycine, valine, tyrosine and lysine residues at positions 5, 7, 17 and 37, respectively. In-vitro lipid-transfer assays reveal that the four proteins catalyze the transfer of phosphatidylcholine from liposomes towards mitochondria with an efficiency similar or higher than that of a purified maize lipid-transfer protein.